Recombinant JCV Polyomavirus Major Capsid VP1 Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-11548P

Recombinant JCV Polyomavirus Major Capsid VP1 Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-11548P
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Product Overview

Accession P18546
Synonym Capsid protein VP1
Description Recombinant JCV Polyomavirus Major Capsid VP1 Protein (Tagged) was expressed in Mammalian. It is a Protein fragment
Source Mammalian
AA Sequence MAPPAKRARGLTLPGYKYLGPGNSLDQGEPTNPSDAAAKEHDEAYDKYIK SGKNPYFYFSAADEKFIKETEHAKDYGGKIGHYFFRAKRAFAPKLSETDS PTTSQQPEVRRSPRKHPGSKPPGKRPAPRHIFINLAKKKAKGTSNTNSNS MSENVEQHNPINAGTELSATGNESGGGGGGGGGRGAGGVGVSTGTFNNQT EFQYLGE
Purity >85% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Lyophilised
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and putative nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus.
Subcellular Location Virion. Host nucleus.
Protein Families Parvoviridae capsid protein family
Database References

Gene Functions References

  1. Data show the expressed VP2 caspid protein was secreted on the cell surface in Lactobacillus casei. PMID: 17460908

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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